ID   GFA_SORMK               Reviewed;         237 AA.
AC   D1ZK87; F7W9V3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Putative glutathione-dependent formaldehyde-activating enzyme;
DE            EC=4.4.1.22;
DE   AltName: Full=S-(hydroxymethyl)glutathione synthase;
GN   ORFNames=SMAC_08712;
OS   Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX   NCBI_TaxID=771870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RX   PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA   Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K.,
RA   Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S.,
RA   Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.;
RT   "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT   Sordaria macrospora, a model organism for fungal morphogenesis.";
RL   PLoS Genet. 6:E1000891-E1000891(2010).
CC   -!- FUNCTION: Catalyzes the condensation of formaldehyde and glutathione to
CC       S-hydroxymethylglutathione. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-(hydroxymethyl)glutathione = formaldehyde + glutathione;
CC         Xref=Rhea:RHEA:22488, ChEBI:CHEBI:16842, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:58758; EC=4.4.1.22;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU01239};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU01239};
CC   -!- PATHWAY: One-carbon metabolism; formaldehyde degradation; formate from
CC       formaldehyde (glutathione route): step 1/3.
CC   -!- SIMILARITY: Belongs to the Gfa family. {ECO:0000305}.
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DR   EMBL; CABT02000055; CCC05220.1; -; Genomic_DNA.
DR   RefSeq; XP_003347275.1; XM_003347227.1.
DR   AlphaFoldDB; D1ZK87; -.
DR   SMR; D1ZK87; -.
DR   STRING; 771870.D1ZK87; -.
DR   EnsemblFungi; CCC05220; CCC05220; SMAC_08712.
DR   GeneID; 10804699; -.
DR   KEGG; smp:SMAC_08712; -.
DR   VEuPathDB; FungiDB:SMAC_08712; -.
DR   eggNOG; ENOG502SKH9; Eukaryota.
DR   HOGENOM; CLU_090716_0_0_1; -.
DR   InParanoid; D1ZK87; -.
DR   OMA; ECGTHMY; -.
DR   OrthoDB; 1326510at2759; -.
DR   UniPathway; UPA00562; UER00621.
DR   Proteomes; UP000001881; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051907; F:S-(hydroxymethyl)glutathione synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046294; P:formaldehyde catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR006913; CENP-V/GFA.
DR   InterPro; IPR011057; Mss4-like_sf.
DR   Pfam; PF04828; GFA; 1.
DR   SUPFAM; SSF51316; SSF51316; 1.
DR   PROSITE; PS51891; CENP_V_GFA; 1.
PE   3: Inferred from homology;
KW   Lyase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..237
FT                   /note="Putative glutathione-dependent formaldehyde-
FT                   activating enzyme"
FT                   /id="PRO_0000406166"
FT   DOMAIN          38..152
FT                   /note="CENP-V/GFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT   BINDING         42
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT   BINDING         44
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT   BINDING         114
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT   BINDING         117
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
SQ   SEQUENCE   237 AA;  25193 MW;  8233A3EFFDE47DB6 CRC64;
     MTAALSSEIS LHPLLDNLPS SASTTTKQEE PSLPALPITL ICHCPPSSSP GPIKVTLTNQ
     ILHNHACGCS KCWKPSGALF SVVGVVPSSG LSVIANAEKL EVVDENATIQ RWKCKECGVH
     LYGRIEKQHP FRGLDFVHGE LALGQSGGSE GEGENEGGGL GEGKVEFAAF VSSIIEGGFE
     PHAHANGDEG KGGNIKQVRD RLREIFGEKV YDCLSPSLMD VIAEWEGRRS GKLKAVL